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Protein

tRNA (guanine-N(7)-)-methyltransferase

Gene

trmB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.

Catalytic activityi

S-adenosyl-L-methionine + guanine(46) in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(46) in tRNA.1 Publication

Pathway:iN(7)-methylguanine-tRNA biosynthesis

This protein is involved in the pathway N(7)-methylguanine-tRNA biosynthesis, which is part of tRNA modification.
View all proteins of this organism that are known to be involved in the pathway N(7)-methylguanine-tRNA biosynthesis and in tRNA modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441S-adenosyl-L-methionineBy similarity
Binding sitei69 – 691S-adenosyl-L-methionineBy similarity
Binding sitei96 – 961S-adenosyl-L-methionineBy similarity
Active sitei118 – 1181By similarity
Binding sitei118 – 1181S-adenosyl-L-methionineBy similarity
Binding sitei122 – 1221SubstrateBy similarity
Binding sitei154 – 1541SubstrateBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciBSUB:BSU29900-MONOMER.
BRENDAi2.1.1.33. 658.
UniPathwayiUPA00989.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (guanine-N(7)-)-methyltransferase (EC:2.1.1.33)
Alternative name(s):
BsTrmB
tRNA (guanine(46)-N(7))-methyltransferase
tRNA(m7G46)-methyltransferase
Gene namesi
Name:trmB
Synonyms:ytmQ
Ordered Locus Names:BSU29900
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU29900. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213tRNA (guanine-N(7)-)-methyltransferasePRO_0000171295Add
BLAST

Proteomic databases

PaxDbiO34522.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100016306.

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 156Combined sources
Turni16 – 194Combined sources
Helixi24 – 274Combined sources
Helixi31 – 355Combined sources
Beta strandi41 – 455Combined sources
Helixi51 – 599Combined sources
Beta strandi63 – 686Combined sources
Helixi72 – 8413Combined sources
Beta strandi88 – 936Combined sources
Helixi97 – 993Combined sources
Helixi100 – 1034Combined sources
Beta strandi111 – 1166Combined sources
Helixi123 – 1286Combined sources
Helixi133 – 14311Combined sources
Beta strandi148 – 1547Combined sources
Helixi156 – 16914Combined sources
Beta strandi172 – 1798Combined sources
Helixi180 – 1823Combined sources
Helixi194 – 1963Combined sources
Beta strandi197 – 2015Combined sources
Beta strandi205 – 2106Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FCAX-ray2.10A/B1-213[»]
ProteinModelPortaliO34522.
SMRiO34522. Positions 10-213.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34522.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni124 – 1296Interaction with RNASequence Analysis
Regioni191 – 1944Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0220.
HOGENOMiHOG000251689.
InParanoidiO34522.
KOiK03439.
OMAiAHPEINY.
OrthoDBiEOG6K6VBC.
PhylomeDBiO34522.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01057. tRNA_methyltr_TrmB.
InterProiIPR029063. SAM-dependent_MTases.
IPR003358. tRNA_(Gua-N-7)_MeTrfase_Trmb.
[Graphical view]
PfamiPF02390. Methyltransf_4. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00091. TIGR00091. 1 hit.
PROSITEiPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O34522-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRMRHKPWAD DFLAENADIA ISNPADYKGK WNTVFGNDNP IHIEVGTGKG
60 70 80 90 100
QFISGMAKQN PDINYIGIEL FKSVIVTAVQ KVKDSEAQNV KLLNIDADTL
110 120 130 140 150
TDVFEPGEVK RVYLNFSDPW PKKRHEKRRL TYSHFLKKYE EVMGKGGSIH
160 170 180 190 200
FKTDNRGLFE YSLKSFSEYG LLLTYVSLDL HNSNLEGNIM TEYEEKFSAL
210
GQPIYRAEVE WRT
Length:213
Mass (Da):24,504
Last modified:January 1, 1998 - v1
Checksum:i28C34F163EB2DD69
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008220 Genomic DNA. Translation: AAC00285.1.
AL009126 Genomic DNA. Translation: CAB14968.1.
PIRiB69997.
RefSeqiNP_390868.1. NC_000964.3.
WP_004398646.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14968; CAB14968; BSU29900.
GeneIDi936447.
KEGGibsu:BSU29900.
PATRICi18977886. VBIBacSub10457_3131.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008220 Genomic DNA. Translation: AAC00285.1.
AL009126 Genomic DNA. Translation: CAB14968.1.
PIRiB69997.
RefSeqiNP_390868.1. NC_000964.3.
WP_004398646.1. NZ_JNCM01000036.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FCAX-ray2.10A/B1-213[»]
ProteinModelPortaliO34522.
SMRiO34522. Positions 10-213.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100016306.

Proteomic databases

PaxDbiO34522.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14968; CAB14968; BSU29900.
GeneIDi936447.
KEGGibsu:BSU29900.
PATRICi18977886. VBIBacSub10457_3131.

Organism-specific databases

GenoListiBSU29900. [Micado]

Phylogenomic databases

eggNOGiCOG0220.
HOGENOMiHOG000251689.
InParanoidiO34522.
KOiK03439.
OMAiAHPEINY.
OrthoDBiEOG6K6VBC.
PhylomeDBiO34522.

Enzyme and pathway databases

UniPathwayiUPA00989.
BioCyciBSUB:BSU29900-MONOMER.
BRENDAi2.1.1.33. 658.

Miscellaneous databases

EvolutionaryTraceiO34522.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01057. tRNA_methyltr_TrmB.
InterProiIPR029063. SAM-dependent_MTases.
IPR003358. tRNA_(Gua-N-7)_MeTrfase_Trmb.
[Graphical view]
PfamiPF02390. Methyltransf_4. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00091. TIGR00091. 1 hit.
PROSITEiPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
    Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
    Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Crystal structure of Bacillus subtilis TrmB, the tRNA (m7G46) methyltransferase."
    Zegers I., Gigot D., van Vliet F., Tricot C., Aymerich S., Bujnicki J.M., Kosinski J., Droogmans L.
    Nucleic Acids Res. 34:1925-1934(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), CATALYTIC ACTIVITY.
    Strain: 168.

Entry informationi

Entry nameiTRMB_BACSU
AccessioniPrimary (citable) accession number: O34522
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 1, 1998
Last modified: July 22, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.